ID COX2_MARPO Reviewed; 251 AA. AC P26857; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 3. DT 13-SEP-2023, entry version 119. DE RecName: Full=Cytochrome c oxidase subunit 2; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide II; GN Name=COX2; Synonyms=COXII; OS Marchantia polymorpha (Common liverwort) (Marchantia aquatica). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta; OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia. OX NCBI_TaxID=3197; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1731062; DOI=10.1016/0022-2836(92)90708-r; RA Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K., RA Kanegae T., Ogura Y., Kohchi T., Ohyama K.; RT "Gene organization deduced from the complete sequence of liverwort RT Marchantia polymorpha mitochondrial DNA. A primitive form of plant RT mitochondrial genome."; RL J. Mol. Biol. 223:1-7(1992). CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00410}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000250|UniProtKB:P00410}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000250|UniProtKB:P00410}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P00410}; CC Note=Binds a dinuclear copper A center per subunit. CC {ECO:0000250|UniProtKB:P00410}; CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of a catalytic core of 3 subunits and CC several supernumerary subunits. The complex exists as a monomer or a CC dimer and forms supercomplexes (SCs) in the inner mitochondrial CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00410}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00410}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M68929; AAC09432.1; -; Genomic_DNA. DR PIR; S25950; S25950. DR RefSeq; NP_054434.1; NC_001660.1. DR AlphaFoldDB; P26857; -. DR SMR; P26857; -. DR GeneID; 2702479; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR CDD; cd13912; CcO_II_C; 1. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1. DR InterPro; IPR045187; CcO_II. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR034210; CcO_II_C. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR014222; Cyt_c_oxidase_su2. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf. DR NCBIfam; TIGR02866; CoxB; 1. DR PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1. DR PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR SUPFAM; SSF49503; Cupredoxins; 1. DR SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 1. DR PROSITE; PS00078; COX2; 1. DR PROSITE; PS50857; COX2_CUA; 1. DR PROSITE; PS50999; COX2_TM; 1. PE 3: Inferred from homology; KW Copper; Electron transport; Magnesium; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain; KW Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..251 FT /note="Cytochrome c oxidase subunit 2" FT /id="PRO_0000183631" FT TOPO_DOM 1..39 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 61..75 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255" FT TRANSMEM 76..104 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 105..251 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT BINDING 184 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 219 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 219 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 221 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with subunit 1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 223 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 223 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 227 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 230 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" SQ SEQUENCE 251 AA; 28894 MW; 1A6527DB9503278A CRC64; MNLIWIFPIA FCDAAEPWQL GFQDPATPMM QGIIDLHNDI FFFLIVILIF VLWMLVRALW HFHYKRNPIP ERIVHGTTIE IIWTIFPSII LMFIAIPSFA LLYSMDEVVD PAITIKAIGH QWYWTYEYSD YNSSDEQSLT FDSYMIPEDD LELGQLRLLE VDNRVVVPAK THLRMIITSA DVLHSWAVPS LGVKCDAVPG RLNQTSIFIK REGVYYGQCS ELCGTNHGFM PIVVEAVSLD DYVSWVSNKL D //